Evidence map›Paper›PMID 8756646›Full record

ArticleMolecular and cellular biology1996

The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases.

S Brill, S Li, C W Lyman, D M Church, J J Wasmuth, L Weissbach, A Bernards, A J Snijders

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
7.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

103 citing papers in PubMed, 259 citations in OpenAlex.

  1. Article
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  3. Queue Gaps Among the IQGAPs inInternational journal of molecular sciences · 2026
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43 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

S BrillMassachusetts General Hospital Cancer Centre, Harvard Medical School, Charlestown, Massachusetts 02129, USA.
S Li
C W Lyman
D M Church
J J Wasmuth
L Weissbach
A Bernards
A J Snijders
Harvard University · USUniversity of California, Irvine · US

Funding

NUCLEIC ACID AND PROTEIN METABOLISM IN CARTILAGER01AR016265 · NIAMS · MASSACHUSETTS GENERAL HOSPITAL · PI MANKIN, HENRY J · 1986 to 2001
$639k
NEUROFIBROMATOSIS-1 MUTATIONS AND NEUROBLASTOMAR01NS031747 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI BERNARDS, ANDRE · 1994 to 1996
–
NIAMS NIH HHS AR16265E21NINDS NIH HHS NS31747
6 · The paper itself

Abstract

We previously described IQGAP1 as a human protein related to a putative Ras GTPase-activating protein (RasGAP) from the fission yeast Schizosaccharomyces pombe. Here we report the identification of a liver-specific human protein that is 62% identical to IQGAP1. Like IQGAP1, the novel IQGAP2 protein harbors an N-terminal calponin homology motif which functions as an F-actin binding domain in members of the spectrin, filamin, and fimbrin families. Both IQGAPs also harbor several copies of a novel 50- to 55-amino-acid repeat, a single WW domain, and four IQ motifs and have 25% sequence identity with almost the entire S. pombe sar1 RasGAP homolog. As predicted by the presence of IQ motifs, IQGAP2 binds calmodulin. However, neither full-length nor truncated IQGAP2 stimulated the GTPase activity of Ras or its close relatives. Instead, IQGAP2 binds Cdc42 and Racl but not RhoA. This interaction involves the C-terminal half of IQGAP2 and appears to be independent of the nucleotide binding status of the GTPases. Although IQGAP2 shows no GAP activity towards Cdc42 and Rac1, the protein did inhibit both the intrinsic and RhoGAP-stimulated GTP hydrolysis rates of Cdc42 and Rac1, suggesting an alternative mechanism via which IQGAPs might modulate signaling by these GTPases. Since IQGAPs harbor a potential actin binding domain, they could play roles in the Cdc42 and Rac1 controlled generation of specific actin structures.

Indexed as

ras GTPase-Activating ProteinsActinsAmino Acid SequenceBase SequenceCalmodulinCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesHumansMolecular Sequence DataProtein BindingProtein Structure, Tertiaryrac GTP-Binding ProteinsRecombinant Fusion ProteinsActinsCalmodulinCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesIQGAP2 protein, humanrac GTP-Binding Proteinsras GTPase-Activating ProteinsRecombinant Fusion Proteins

Identifiers

PMID8756646
PMCPMC231489
OpenAlexW2164550657

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.